Chromosome instability protein 1

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functionⁱ

Miscellaneous

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functionⁱ

• beta-tubulin binding Source: SGD <p>Inferred from Sequence or Structural Similarity<br />Used for any analysis based on sequence alignment, structure comparison, or evaluation of sequence features such as composition.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iss">GO evidence code guide</a></p> Inferred from sequence or structural similarityⁱ
  • "Pathway leading to correctly folded beta-tubulin."
    Tian G., Huang Y., Rommelaere H., Vandekerckhove J., Ampe C., Cowan N.J.
    Cell 86:287-296(1996) [PubMed] [Europe PMC] [Abstract]
• GTPase activator activity Source: GO_Central <p>Inferred from Biological aspect of Ancestor</p> <p>A type of phylogenetic evidence whereby an aspect of a descendent is inferred through the characterization of an aspect of a ancestral gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iba">GO evidence code guide</a></p> Inferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]

GO - Biological processⁱ

• microtubule cytoskeleton organization Source: GO_CentralInferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• post-chaperonin tubulin folding pathway Source: InterPro
• protein folding Source: SGD <p>Inferred from Genetic Interaction</p> <p>Used to describe "traditional" genetic interactions such as suppressors and synthetic lethals as well as other techniques such as functional complementation, rescue experiments, or inferences about a gene drawn from the phenotype of a mutation in a different gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#igi">GO evidence code guide</a></p> Inferred from genetic interactionⁱ
  • "Yeast mutants sensitive to antimicrotubule drugs define three genes that affect microtubule function."
    Stearns T., Hoyt M.A., Botstein D.
    Genetics 124:251-262(1990) [PubMed] [Europe PMC] [Abstract]
• tubulin complex assembly Source: SGD <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ
  • "Saccharomyces cerevisiae PAC2 functions with CIN1, 2 and 4 in a pathway leading to normal microtubule stability."
    Hoyt M.A., Macke J.P., Roberts B.T., Geiser J.R.
    Genetics 146:849-857(1997) [PubMed] [Europe PMC] [Abstract]

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyⁱ

Organism-specific databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingⁱ

Molecule processing

Proteomic databases

PTM databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactionⁱ

GO - Molecular functionⁱ

• beta-tubulin binding Source: SGDInferred from sequence or structural similarityⁱ
  • "Pathway leading to correctly folded beta-tubulin."
    Tian G., Huang Y., Rommelaere H., Vandekerckhove J., Ampe C., Cowan N.J.
    Cell 86:287-296(1996) [PubMed] [Europe PMC] [Abstract]

Protein-protein interaction databases

Miscellaneous databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structureⁱ

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsⁱ

Phylogenomic databases

Family and domain databases

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequenceⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusⁱ: Complete.

        10         20         30         40         50
MNNIRALLDS IQSGVQTVSP EKHQQTIAAI NKFQDDPALL DTILPRCVPL 
        60         70         80         90        100
LTKSFFCMSQ RDQKLVAELF YNLDKISHSK VLKSLDTSIF RLNEILNYLQ 
       110        120        130        140        150
DRASPSSFSD VLCVYLNLSW LSVILLSPYA FKDKFNKTLQ VSSRFENYPI 
       160        170        180        190        200
CIPPINKIKA VLYFKNFTDA FDQLPEREQA NVPFLNQFLK LFIQSSEKAN 
       210        220        230        240        250
YYFSNENLRH LQQVALSNDG IKLLPKLFQI SFNHGSHDIL DAIVEFFHDH 
       260        270        280        290        300
LSSNSTDTRF QLAHSFAKIA KFLHQADPAS FIELIDYTIE NTVSLLQAPC 
       310        320        330        340        350
DSIDSNELHT SLLIIAEVAL AKILPIDLVD RVLTLIIPKT CHFQKSHFQI 
       360        370        380        390        400
IKGHHIRDST NFIIWSVIRS NRSNSLSPQV LQSLLSHLLI NAFFDPELII 
       410        420        430        440        450
RYSSFAALQE LLGRSNKSLA LNQNDIALIL QANWKDLPRS FEENSGLIRR 
       460        470        480        490        500
LFNPENTSKS AVCVWKVFRD WSFNWNLLEN LHLTTMKLNI DYNLVPLIKS 
       510        520        530        540        550
KLSSPALLQE VLNKAGSSVT QNCQILYLYL KLFENDVNCP KISEICIDIY 
       560        570        580        590        600
QKKIKFQLTT QAKRQFNDNS PELFQIFVIL KYWQLTGQND FNQELFWKFV 
       610        620        630        640        650
DIVSPQKKLN LYNEFIPIIQ QIISQCVSLN YTRIVQLIKS DNELTCRSIC 
       660        670        680        690        700
HMPDQEKMCS LFFSQFPLLS PQSRSLLIGE LDHHWDVRIS LLPSNSYRKF 
       710        720        730        740        750
RNIIINCLDD YTITQQGDVG RLVRIQALKL MQSHPDFLSG DCDSINPKLT 
       760        770        780        790        800
RLLAEPVPEI RKLSYQLLAS ATSQITVLSD SSILNFRHKQ GLSEEFWKGY 
       810        820        830        840        850
AVSAGAIHFT DSQLTSSIDS FIVYYRSLSP SQQLELCHDL IRIIPSAKQI 
       860        870        880        890        900
AESRIRDRNK DPLTGGMRFD TIKFTIHCVK FWTRIMESGL VVLHPNFNFQ 
       910        920        930        940        950
GVFAKFYNLH LLDCTTLRVS VIKFFPFLAI SCYHTMRENA DQKNLSNIIL 
       960        970        980        990       1000
KRLLVLVKRE YAATKSKFMT DQNVALQGMF QIFLELGVTR QLQALQVACQ 
      1010 
KHELANILES DITL                                        

Sequence databases

Genome annotation databases

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsⁱ

• 100% Identity
• 90% Identity
• 50% Identity

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesⁱ

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationⁱ

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousⁱ

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Technical termⁱ

Documents

1. Yeast
   Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
2. Yeast chromosome XV
   Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names